Article
New conformational properties induced by the replacement of Tyr-64 in Desulfovibrio vulgaris Hildenborough ferricytochrome c553 using isotopic exchanges monitored by mass spectrometry.
FEBS letters - 14 Oct 1996
Guy P, Jaquinod M, Rémigy H, Andrieu J P, Gagnon J, Bersch B, Dolla A, Blanchard L, Guerlesquin F, Forest E
Abstract excerpt
In order to study the conformational stability induced by the replacement of Tyr-64 in Desulfovibrio vulgaris Hildenborough (DvH) cytochrome c553, fast peptic digestion of deuterated protein followed by separation and measurement of related peptides using liquid chromatography coupled to electros...
Topics
- Cytochrome c Group
- Desulfovibrio vulgaris
- Deuterium
- Electrons
- Hydrogen Bonding
- Molecular Weight
- Mutation
- Oxidation-Reduction
- Peptide Fragments
- Protein Conformation
- Solvents
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Tyrosine